title: Purification of human placental prostaglandin 15-hydroxydehydrogenase.
abstract: The NAD(+)-linked prostaglandin 15-hydroxydehydrogenase, which is responsible for the physiological inactivation of prostaglandins by catalysing the first step in the catabolism, was isolated and purified 995-fold from human placenta. The introduction of two new chromatographic steps in the purification procedure is responsible for an achieved specific activity of 1791 mU/mg. The molecular mass of the enzyme, as estimated by fast protein liquid chromatography, was 24,500 dalton. Sodium dodecyl sulphate discontinuous gel electrophoresis of the denatured enzyme revealed a molecular mass of 24,000 dalton. These data suggest that the enzyme consists of a single polypeptide chain.
authors.affiliation: Universitätsfrauenklinik, Münster, F.R.G.
authors.forename: B
authors.initials: B
authors.lastname: Tombach
authors.forename: R
authors.initials: R
authors.lastname: Kusseler
authors.forename: W
authors.initials: W
authors.lastname: Schlegel
mesh_terms: D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D006911:Hydroxyprostaglandin Dehydrogenases / Q000302:isolation & purification*; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011489:Protein Denaturation
chemical_list: D006911:Hydroxyprostaglandin Dehydrogenases; C035859:15-hydroxyprostaglandin dehydrogenase